ID A0A2G5SNB8_9PELO Unreviewed; 237 AA.
AC A0A2G5SNB8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Tetraspanin {ECO:0000256|RuleBase:RU361218};
GN Name=Cni-tsp-6 {ECO:0000313|EMBL:PIC16361.1};
GN Synonyms=Cnig_chr_X.g22995 {ECO:0000313|EMBL:PIC16361.1};
GN ORFNames=B9Z55_022995 {ECO:0000313|EMBL:PIC16361.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC16361.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
CC -!- SIMILARITY: Belongs to the tetraspanin (TM4SF) family.
CC {ECO:0000256|ARBA:ARBA00006840, ECO:0000256|RuleBase:RU361218}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC16361.1}.
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DR EMBL; PDUG01000006; PIC16361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5SNB8; -.
DR STRING; 1611254.A0A2G5SNB8; -.
DR Proteomes; UP000230233; Chromosome x.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR CDD; cd03127; tetraspanin_LEL; 1.
DR Gene3D; 1.10.1450.10; Tetraspanin; 1.
DR InterPro; IPR018499; Tetraspanin/Peripherin.
DR InterPro; IPR000301; Tetraspanin_animals.
DR InterPro; IPR018503; Tetraspanin_CS.
DR InterPro; IPR008952; Tetraspanin_EC2_sf.
DR PANTHER; PTHR19282; TETRASPANIN; 1.
DR PANTHER; PTHR19282:SF459; TETRASPANIN; 1.
DR Pfam; PF00335; Tetraspanin; 1.
DR PIRSF; PIRSF002419; Tetraspanin; 1.
DR PRINTS; PR00259; TMFOUR.
DR SUPFAM; SSF48652; Tetraspanin; 1.
DR PROSITE; PS00421; TM4_1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361218};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
KW Transmembrane {ECO:0000256|RuleBase:RU361218};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361218}.
FT TRANSMEM 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361218"
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361218"
FT TRANSMEM 100..121
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361218"
FT TRANSMEM 202..230
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361218"
SQ SEQUENCE 237 AA; 26072 MW; 510B24FB54E85841 CRC64;
MVKGCGNKCI KYFFWLINLL FFVLGAVIVG LSIWMLVDKN SLTTVASTVK VDLSQVLNQV
NIQQINTFLY VALVIGGALL ILGFFGCCGS CCESVCAISI YFILVLILFV IEVVAIVLYF
VKKTELQQGL TTIWRDELVS KYNTNQQIHQ ALDQLQSSLQ CCGASGCSDY MVYGAFPTSC
QCATLSQQGC ATLLWNAFQT NLIYVAFVGI IVLFVEALAM IFSCIIINAV KAKRNEA
//
